COENZYME MODELS - 19. OXIDATION OF FUROIN BY A FLAVIN IMMOBILIZED IN CATIONIC POLYELECTROLYTES - A FLAVOENZYME MODEL.

Seiji Shinkai

Research output: Contribution to journalArticle

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Abstract

In the reported study, the rate constants for the oxidation of furoin by a flavin (vitamin B//2 analog) immobilized in catonic polymers were evaluated under anaerobic conditions, and the influence of reaction environments was discussed in connection with the enzymatic reactivity. It was found that (1) proton abstraction from furoin which forms the carbanionic intermediate is rate determining in the initial stage of the reaction and is facilitated by the environment of cationic polymers, (2) proton abstraction is efficiently accelerated by added cationic surfactant (CTAB), and (3) N-dodecylbenzohydroxamic acid in aqueous CTAB acts as an excellent proton-abstracting reagent. the polymers with high dodecyl group content served, in all cases, as better oxidizing reagents. As a summary of these conclusions, the importance of hydrophobic environments in flavin-mediated oxidation was emphasized.

Original languageEnglish
Pages (from-to)3905-3912
Number of pages8
JournalJournal of polymer science. Part A-1, Polymer chemistry
Volume17
Issue number12
Publication statusPublished - Jan 1 1979
Externally publishedYes

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Coenzymes
Polyelectrolytes
Protons
Oxidation
Polymers
Cationic surfactants
Vitamins
Rate constants
Acids

All Science Journal Classification (ASJC) codes

  • Engineering(all)

Cite this

COENZYME MODELS - 19. OXIDATION OF FUROIN BY A FLAVIN IMMOBILIZED IN CATIONIC POLYELECTROLYTES - A FLAVOENZYME MODEL. / Shinkai, Seiji.

In: Journal of polymer science. Part A-1, Polymer chemistry, Vol. 17, No. 12, 01.01.1979, p. 3905-3912.

Research output: Contribution to journalArticle

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